Nicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other, nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD+ and NADH (H for hydrogen), respectively.
Nicotinamide adenine dinucleotide phosphate, abbreviated NADP+ or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). NADPH is the reduced form, whereas NADP+ is the oxidized form. NADP+ is used by all forms of cellular life.
Cyclic ADP-ribose, frequently abbreviated as cADPR, is a cyclic adenine nucleotide (like cAMP) with two phosphate groups present on 5' OH of the adenosine (like ADP), further connected to another ribose at the 5' position, which, in turn, closes the cycle by glycosidic bonding to the nitrogen 1 (N1) of the same adenine base (whose position N9 has the glycosidic bond to the other ribose). The N1-glycosidic bond to adenine is what distinguishes cADPR from ADP-ribose (ADPR), the non-cyclic analog. cADPR is produced from nicotinamide adenine dinucleotide (NAD+) by ADP-ribosyl cyclases (EC 3.2.2.5) as part of a second messenger system.
ADP-ribosylation is the addition of one or more ADP-ribose moieties to a protein. It is a reversible post-translational modification that is involved in many cellular processes, including cell signaling, DNA repair, gene regulation and apoptosis. Improper ADP-ribosylation has been implicated in some forms of cancer. It is also the basis for the toxicity of bacterial compounds such as cholera toxin, diphtheria toxin, and others.
D-Xylose is a five-carbon aldose that can be catabolized or metabolized into useful products by a variety of organisms.
In enzymology, a phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase (EC 3.2.2.6) is a bifunctional enzyme that catalyzes the chemical reaction
In enzymology, a NAD(P)+-protein-arginine ADP-ribosyltransferase (EC 2.4.2.31) is an enzyme that catalyzes the chemical reaction using nicotinamide adenine dinucleotide
In enzymology, a nicotinate phosphoribosyltransferase (EC 6.3.4.21) is an enzyme that catalyzes the chemical reaction
In enzymology, a gluconokinase is an enzyme that catalyzes the chemical reaction
In enzymology, a glycerate kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a hydroxyethylthiazole kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a polynucleotide 5'-hydroxyl-kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a protein-histidine pros-kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a protein-histidine tele-kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a ribose 1,5-bisphosphate phosphokinase is an enzyme that catalyzes the chemical reaction
In enzymology, a tRNA nucleotidyltransferase is an enzyme that catalyzes the chemical reaction
In molecular biology, the Macro domain or A1pp domain is a module of about 180 amino acids which can bind ADP-ribose, an NAD metabolite, or related ligands. Binding to ADP-ribose can be either covalent or non-covalent: in certain cases it is believed to bind non-covalently, while in other cases it appears to bind both non-covalently through a zinc finger motif, and covalently through a separate region of the protein.
TRNA-dihydrouridine16/17 synthase (NAD(P)+) (EC 1.3.1.88, Dus1p, tRNA-dihydrouridine synthase 1) is an enzyme with systematic name tRNA-5,6-dihydrouracil16/17:NAD(P)+ oxidoreductase. This enzyme catalyses the following chemical reaction
ADP-ribose 1′′-phosphate phosphatase (EC 3.1.3.84, POA1, Appr1p phosphatase, Poa1p) is an enzyme with systematic name ADP-D-ribose 1′′-phosphate phosphohydrolase. This enzyme catalyses the following chemical reaction
